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Protein

Dual specificity protein phosphatase 14

Gene

DUSP14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei111 – 1111Phosphocysteine intermediatePROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. protein tyrosine/serine/threonine phosphatase activity Source: GO_Central
  4. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. peptidyl-tyrosine dephosphorylation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 14 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
MKP-1-like protein tyrosine phosphatase
Short name:
MKP-L
Mitogen-activated protein kinase phosphatase 6
Short name:
MAP kinase phosphatase 6
Short name:
MKP-6
Gene namesi
Name:DUSP14
Synonyms:MKP6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:17007. DUSP14.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27523.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 198198Dual specificity protein phosphatase 14PRO_0000094822Add
BLAST

Proteomic databases

PaxDbiO95147.
PeptideAtlasiO95147.
PRIDEiO95147.

PTM databases

DEPODiO95147.
PhosphoSiteiO95147.

Expressioni

Gene expression databases

BgeeiO95147.
CleanExiHS_DUSP14.
ExpressionAtlasiO95147. baseline and differential.
GenevestigatoriO95147.

Organism-specific databases

HPAiHPA019911.

Interactioni

Subunit structurei

Interacts with CD28.1 Publication

Protein-protein interaction databases

BioGridi116255. 20 interactions.
IntActiO95147. 1 interaction.
STRINGi9606.ENSP00000292964.

Structurei

Secondary structure

1
198
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 315Combined sources
Beta strandi34 – 374Combined sources
Helixi39 – 424Combined sources
Helixi45 – 506Combined sources
Beta strandi55 – 584Combined sources
Beta strandi61 – 633Combined sources
Beta strandi71 – 755Combined sources
Helixi86 – 894Combined sources
Helixi90 – 10213Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi112 – 1165Combined sources
Helixi117 – 13014Combined sources
Helixi134 – 14411Combined sources
Helixi152 – 16615Combined sources
Beta strandi173 – 1764Combined sources
Beta strandi179 – 1824Combined sources
Helixi183 – 1897Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WGPX-ray1.88A/B2-191[»]
ProteinModelPortaliO95147.
SMRiO95147. Positions 24-191.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95147.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 15666Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000233766.
HOVERGENiHBG051422.
InParanoidiO95147.
KOiK14165.
OMAiLMPYWGL.
OrthoDBiEOG7PK90H.
PhylomeDBiO95147.
TreeFamiTF316009.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95147-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSRGHSTLP RTLMAPRMIS EGDIGGIAQI TSSLFLGRGS VASNRHLLQA
60 70 80 90 100
RGITCIVNAT IEIPNFNWPQ FEYVKVPLAD MPHAPIGLYF DTVADKIHSV
110 120 130 140 150
SRKHGATLVH CAAGVSRSAT LCIAYLMKFH NVCLLEAYNW VKARRPVIRP
160 170 180 190
NVGFWRQLID YERQLFGKST VKMVQTPYGI VPDVYEKESR HLMPYWGI
Length:198
Mass (Da):22,255
Last modified:April 30, 1999 - v1
Checksum:i6AAFAE1B3A24F9AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038844 mRNA. Translation: AAD02105.1.
AF120032 mRNA. Translation: AAF28861.1.
BC000370 mRNA. Translation: AAH00370.1.
BC001894 mRNA. Translation: AAH01894.1.
BC004448 mRNA. Translation: AAH04448.1.
CCDSiCCDS11320.1.
RefSeqiNP_008957.1. NM_007026.3.
XP_005257034.1. XM_005256977.1.
XP_006725363.1. XM_006725300.1.
UniGeneiHs.91448.

Genome annotation databases

EnsembliENST00000613659; ENSP00000484091; ENSG00000276023.
ENST00000614294; ENSP00000478406; ENSG00000275932.
ENST00000614411; ENSP00000477653; ENSG00000276023.
ENST00000617516; ENSP00000478595; ENSG00000276023.
GeneIDi11072.
KEGGihsa:11072.
UCSCiuc002hnx.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038844 mRNA. Translation: AAD02105.1.
AF120032 mRNA. Translation: AAF28861.1.
BC000370 mRNA. Translation: AAH00370.1.
BC001894 mRNA. Translation: AAH01894.1.
BC004448 mRNA. Translation: AAH04448.1.
CCDSiCCDS11320.1.
RefSeqiNP_008957.1. NM_007026.3.
XP_005257034.1. XM_005256977.1.
XP_006725363.1. XM_006725300.1.
UniGeneiHs.91448.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WGPX-ray1.88A/B2-191[»]
ProteinModelPortaliO95147.
SMRiO95147. Positions 24-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116255. 20 interactions.
IntActiO95147. 1 interaction.
STRINGi9606.ENSP00000292964.

Chemistry

BindingDBiO95147.
ChEMBLiCHEMBL1764941.

PTM databases

DEPODiO95147.
PhosphoSiteiO95147.

Proteomic databases

PaxDbiO95147.
PeptideAtlasiO95147.
PRIDEiO95147.

Protocols and materials databases

DNASUi11072.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000613659; ENSP00000484091; ENSG00000276023.
ENST00000614294; ENSP00000478406; ENSG00000275932.
ENST00000614411; ENSP00000477653; ENSG00000276023.
ENST00000617516; ENSP00000478595; ENSG00000276023.
GeneIDi11072.
KEGGihsa:11072.
UCSCiuc002hnx.2. human.

Organism-specific databases

CTDi11072.
GeneCardsiGC17P035850.
HGNCiHGNC:17007. DUSP14.
HPAiHPA019911.
MIMi606618. gene.
neXtProtiNX_O95147.
PharmGKBiPA27523.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000233766.
HOVERGENiHBG051422.
InParanoidiO95147.
KOiK14165.
OMAiLMPYWGL.
OrthoDBiEOG7PK90H.
PhylomeDBiO95147.
TreeFamiTF316009.

Miscellaneous databases

ChiTaRSiDUSP14. human.
EvolutionaryTraceiO95147.
GenomeRNAii11072.
NextBioi42090.
PROiO95147.
SOURCEiSearch...

Gene expression databases

BgeeiO95147.
CleanExiHS_DUSP14.
ExpressionAtlasiO95147. baseline and differential.
GenevestigatoriO95147.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MKP-L, a novel MKP-1 like protein tyrosine phosphatase."
    Yuan Y., Suphapeetiporn K., Sun H.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Negative-feedback regulation of CD28 costimulation by a novel mitogen-activated protein kinase phosphatase, MKP6."
    Marti F., Krause A., Post N.H., Lyddane C., Dupont B., Sadelain M., King P.D.
    J. Immunol. 166:197-206(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Overproduction, purification and structure determination of human dual-specificity phosphatase 14."
    Lountos G.T., Tropea J.E., Cherry S., Waugh D.S.
    Acta Crystallogr. D 65:1013-1020(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 2-191 IN COMPLEX WITH PHOSPHATE, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiDUS14_HUMAN
AccessioniPrimary (citable) accession number: O95147
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 22, 2002
Last sequence update: April 30, 1999
Last modified: March 3, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.